Brucella sp. bind to sialic acid residues on human and animal red blood cells

FEMS Microbiol Lett. 2002 Aug 6;213(2):219-24. doi: 10.1111/j.1574-6968.2002.tb11309.x.

Abstract

We report that Brucella abortus and Brucella melitensis agglutinate human (A+ and B+), hamster and rabbit erythrocytes, a heretofore undescribed feature in this genus. This activity was associated with a 29-kDa surface protein (SP29) that bound selectively to these erythrocytes and this binding was inhibited by rabbit anti-SP29 antibodies. Hemagglutination was inhibited by pretreatment of erythrocytes with neuraminidase and by preincubation of B. abortus with chondroitin sulfate, N-acetylneuraminic acid and N-acetylneuramin-lactose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigen-Antibody Reactions
  • Bacterial Adhesion*
  • Brucella / immunology*
  • Brucella abortus / immunology
  • Chondroitin Sulfates / pharmacology
  • Cricetinae
  • Erythrocytes / drug effects
  • Erythrocytes / immunology*
  • Erythrocytes / metabolism
  • Hemagglutination Tests
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid / metabolism*
  • Neuraminidase / pharmacology
  • Rabbits
  • Receptors, Cell Surface / metabolism

Substances

  • Receptors, Cell Surface
  • sialic acid receptor
  • Chondroitin Sulfates
  • Neuraminidase
  • N-Acetylneuraminic Acid